ID DLDH1_PSEPU Reviewed; 459 AA. AC P09063; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 04-NOV-2026, entry version 176. DE RecName: Full=Dihydrolipoyl dehydrogenase; DE EC=1.8.1.4 {ECO:0000250|UniProtKB:P09624}; DE AltName: Full=Dihydrolipoamide dehydrogenase; DE AltName: Full=E3 component of branched-chain alpha-keto acid dehydrogenase complex; DE AltName: Full=LPD-Val; GN Name=lpdV {ECO:0000303|PubMed:3046941}; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=G2; RX PubMed=3046941; DOI=10.1111/j.1432-1033.1988.tb14264.x; RA Burns G., Brown T., Hatter K., Sokatch J.R.; RT "Comparison of the amino acid sequences of the transacylase components of RT branched chain oxoacid dehydrogenase of Pseudomonas putida, and the RT pyruvate and 2-oxoglutarate dehydrogenases of Escherichia coli."; RL Eur. J. Biochem. 176:165-169(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=G2; RX PubMed=2917566; DOI=10.1111/j.1432-1033.1989.tb14521.x; RA Burns G., Brown T., Hatter K., Sokatch J.R.; RT "Sequence analysis of the lpdV gene for lipoamide dehydrogenase of RT branched-chain-oxoacid dehydrogenase of Pseudomonas putida."; RL Eur. J. Biochem. 179:61-69(1989). RN [3] {ECO:0007744|PDB:1LVL} RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NAD AND FAD, COFACTOR, SUBUNIT, AND RP DISULFIDE BOND. RX PubMed=1325638; DOI=10.1002/prot.340130406; RA Mattevi A., Obmolova G., Sokatsch J.R., Betzel C., Hol W.G.J.; RT "The refined crystal structure of Pseudomonas putida lipoamide RT dehydrogenase complexed with NAD+ at 2.45-A resolution."; RL Proteins 13:336-351(1992). CC -!- FUNCTION: Component of the branched-chain alpha-keto dehydrogenase CC complex, which catalyzes the overall conversion of alpha-keto acids CC derived from the branched-chain amino-acids valine, leucine and CC isoleucine to acyl-CoA and CO(2). The complex contains multiple copies CC of three enzymatic components: branched-chain alpha-keto acid CC decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide CC dehydrogenase (E3). {ECO:0000250|UniProtKB:P54533}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = N(6)- CC [(R)-lipoyl]-L-lysyl-[protein] + NADH + H(+); Xref=Rhea:RHEA:15045, CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, CC ChEBI:CHEBI:83100; EC=1.8.1.4; CC Evidence={ECO:0000250|UniProtKB:P09624}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:1325638}; CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:1325638}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1325638}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC {ECO:0000250|UniProtKB:P09624}. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M57613; AAA65618.1; -; Genomic_DNA. DR PIR; S02139; DEPSLP. DR RefSeq; WP_027609417.1; NZ_AP022324.1. DR PDB; 1LVL; X-ray; 2.45 A; A=2-459. DR AlphaFoldDB; P09063; -. DR SMR; P09063; -. DR DrugBank; DB03147; Flavin adenine dinucleotide. DR eggNOG; COG1249; Bacteria. DR EvolutionaryTrace; P09063; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase (NADH) activity; ISS:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:TreeGrafter. DR FunFam; 3.30.390.30:FF:000001; Dihydrolipoyl dehydrogenase; 1. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2. DR InterPro; IPR050151; Class-I_Pyr_Nuc-Dis_Oxidored. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf. DR InterPro; IPR006258; Lipoamide_DH. DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR NCBIfam; TIGR01350; lipoamide_DH; 1. DR PANTHER; PTHR22912:SF160; DIHYDROLIPOYL DEHYDROGENASE; 1. DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; KW Flavoprotein; NAD; Oxidoreductase; Redox-active center. FT CHAIN 1..459 FT /note="Dihydrolipoyl dehydrogenase" FT /id="PRO_0000068038" FT ACT_SITE 438 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P09624" FT BINDING 43 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT BINDING 44 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT BINDING 53 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT BINDING 119 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT BINDING 182 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT BINDING 202 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT BINDING 236 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT BINDING 267 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT BINDING 306 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT BINDING 312 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT BINDING 314 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1325638, FT ECO:0007744|PDB:1LVL" FT DISULFID 44..49 FT /note="Redox-active" FT /evidence="ECO:0000250|UniProtKB:P09624, FT ECO:0007744|PDB:1LVL" FT STRAND 8..12 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 16..28 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 32..35 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 42..47 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 49..67 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 85..109 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 119..123 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 137..141 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 162..165 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 173..178 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 182..194 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 197..201 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 203..208 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 213..226 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 235..240 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 243..247 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 249..251 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 272..275 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 276..278 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 305..308 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 314..328 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 346..354 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 357..362 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 367..373 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 378..382 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 389..395 FT /evidence="ECO:0007829|PDB:1LVL" FT TURN 396..398 FT /evidence="ECO:0007829|PDB:1LVL" FT STRAND 400..408 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 411..413 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 414..424 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 428..432 FT /evidence="ECO:0007829|PDB:1LVL" FT HELIX 443..452 FT /evidence="ECO:0007829|PDB:1LVL" SQ SEQUENCE 459 AA; 48159 MW; 3D60A7DE167D0586 CRC64; MQQTIQTTLL IIGGGPGGYV AAIRAGQLGI PTVLVEGQAL GGTCLNIGCI PSKALIHVAE QFHQASRFTE PSPLGISVAS PRLDIGQSVA WKDGIVDRLT TGVAALLKKH GVKVVHGWAK VLDGKQVEVD GQRIQCEHLL LATGSSSVEL PMLPLGGPVI SSTEALAPKA LPQHLVVVGG GYIGLELGIA YRKLGAQVSV VEARERILPT YDSELTAPVA ESLKKLGIAL HLGHSVEGYE NGCLLANDGK GGQLRLEADR VLVAVGRRPR TKGFNLECLD LKMNGAAIAI DERCQTSMHN VWAIGDVAGE PMLAHRAMAQ GEMVAEIIAG KARRFEPAAI AAVCFTDPEV VVVGKTPEQA SQQGLDCIVA QFPFAANGRA MSLESKSGFV RVVARRDNHL ILGWQAVGVA VSELSTAFAQ SLEMGACLED VAGTIHAHPT LGEAVQEAAL RALGHALHI //